3.4.22.59: caspase-6
This is an abbreviated version!
For detailed information about caspase-6, go to the full flat file.
Word Map on EC 3.4.22.59
-
3.4.22.59
-
caspases
-
bcl-2
-
alzheimer
-
neurodegenerative
-
pro-apoptotic
-
huntington
-
lamins
-
apoptosis-related
-
parp
-
executioner
-
caspase-dependent
-
anti-apoptotic
-
polyadp-ribose
-
tunel
-
caspase-mediated
-
casps
-
jurkat
-
bid
-
pan-caspase
-
zvad-fmk
-
apaf-1
-
medicine
-
procaspase-3
-
fadd
-
diagnostics
-
fas-associated
-
drug development
-
molecular biology
- 3.4.22.59
-
caspases
- bcl-2
- alzheimer
- neurodegenerative
-
pro-apoptotic
- huntington
- lamins
-
apoptosis-related
- parp
-
executioner
-
caspase-dependent
-
anti-apoptotic
-
polyadp-ribose
-
tunel
-
caspase-mediated
-
casps
-
jurkat
- bid
-
pan-caspase
- zvad-fmk
- apaf-1
- medicine
- procaspase-3
- fadd
- diagnostics
-
fas-associated
- drug development
- molecular biology
Reaction
strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-/- =
Synonyms
apoptotic protease Mch-2, C14.005, Cas6, Casp-6, Casp.6, Casp6, caspase 6, caspase-6, caspase-6A, caspase-6B, Csp-6, Csp6, HLcaspase-6, MCH2, Pfcasp-6, VEIDase
ECTree
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 3.4.22.59 - caspase-6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
proteolytic modification
proteolytic modification
-
viral nucleocapsid protein of transmissible gastroenteritis coronavirus triggers the processing of procaspase 6 in human rectal tumor cell line HRT18jap1
proteolytic modification
-
caspase-6 is inactive until the short 23 amino acid prodomain is removed
proteolytic modification
-
activation through cleavage mainly by caspase-8, partly by caspase-2 and caspase-9
proteolytic modification
-
caspase-6 activates itself through self-processing, processing at either intersubunit linker sites D23, D179 and D193, the prodomain of Casp6 entirely prevents self-processing and activation in vivo but not in vitro, removal of the pro-domain promotes Casp6 activation. Processing of caspase-6 mutants by recombinant caspase-3, overview
proteolytic modification
-
activation by proteolytic self-cleavage, during activation, the N-terminal prodomain is removed by cleavage at a TETD site. Double cleavage in an unstructured linker region at a DVVD and a TEVD site gives rise to a large 20-kDa and a small 10-kDa subunit. The two large p20 and two small p10 subunits then assemble to form the active CASP6 complex
proteolytic modification
-
pro-forms of caspase-6 isozymes need to be proteolytically self-activated. RCasp1-mediated increased processing of pro-Casp6a, while pro-Casp6b inhibits pro-Casp6a activationinto its active subunits